Header list of 1bve.pdb file
Complete list - v 3 2 Bytes
HEADER ASPARTYL PROTEASE 16-JAN-96 1BVE
TITLE HIV-1 PROTEASE-DMP323 COMPLEX IN SOLUTION, NMR, 28 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 PROTEASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.23.16;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: HXB2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS AIDS, POLYPROTEIN, HYDROLASE, ASPARTYL PROTEASE, ENDONUCLEASE, RNA-
KEYWDS 2 DIRECTED DNA POLYMERASE
EXPDTA SOLUTION NMR
NUMMDL 28
AUTHOR T.YAMAZAKI,A.P.HINCK,Y.-X.WANG,L.K.NICHOLSON,D.A.TORCHIA,P.WINGFIELD,
AUTHOR 2 S.J.STAHL,J.D.KAUFMAN,C.CHANG,P.J.DOMAILLE,P.Y.S.LAM
REVDAT 3 03-NOV-21 1BVE 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 24-FEB-09 1BVE 1 VERSN
REVDAT 1 17-AUG-96 1BVE 0
JRNL AUTH T.YAMAZAKI,A.P.HINCK,Y.X.WANG,L.K.NICHOLSON,D.A.TORCHIA,
JRNL AUTH 2 P.WINGFIELD,S.J.STAHL,J.D.KAUFMAN,C.H.CHANG,P.J.DOMAILLE,
JRNL AUTH 3 P.Y.LAM
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE HIV-1 PROTEASE
JRNL TITL 2 COMPLEXED WITH DMP323, A NOVEL CYCLIC UREA-TYPE INHIBITOR,
JRNL TITL 3 DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF PROTEIN SCI. V. 5 495 1996
JRNL REFN ISSN 0961-8368
JRNL PMID 8868486
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BVE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172109.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.1
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 28
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 28
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS ENTRY CONTAINS 1 TO 28 OF 28 MODELS.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 LEU A 5 39.33 -89.56
REMARK 500 1 TRP A 6 59.36 16.28
REMARK 500 1 LEU A 24 95.17 -44.95
REMARK 500 1 GLU A 34 170.68 -45.16
REMARK 500 1 MET A 36 -158.92 -177.80
REMARK 500 1 ARG A 41 44.33 150.04
REMARK 500 1 GLN A 58 94.54 -54.58
REMARK 500 1 GLN A 61 63.48 69.48
REMARK 500 1 LEU A 63 82.91 -64.77
REMARK 500 1 PRO A 79 43.26 -80.31
REMARK 500 1 THR B 4 -105.19 -67.79
REMARK 500 1 LEU B 5 -11.64 -171.88
REMARK 500 1 THR B 12 90.50 -68.26
REMARK 500 1 GLU B 34 153.30 -36.56
REMARK 500 1 MET B 36 -174.12 -177.26
REMARK 500 1 GLN B 58 95.05 -48.02
REMARK 500 1 GLN B 61 59.27 84.95
REMARK 500 1 ALA B 71 100.88 -160.13
REMARK 500 1 PRO B 79 41.86 -81.44
REMARK 500 2 THR A 4 -90.91 -127.71
REMARK 500 2 LEU A 5 29.17 41.63
REMARK 500 2 TRP A 6 51.84 18.07
REMARK 500 2 LEU A 24 96.81 -43.94
REMARK 500 2 LEU A 33 116.35 -169.15
REMARK 500 2 GLU A 34 162.02 -39.35
REMARK 500 2 GLU A 35 156.85 -41.34
REMARK 500 2 MET A 36 -176.94 -179.02
REMARK 500 2 PRO A 39 -163.06 -69.53
REMARK 500 2 ARG A 41 50.44 -109.56
REMARK 500 2 GLN A 58 105.08 -55.06
REMARK 500 2 GLN A 61 61.91 78.29
REMARK 500 2 CYS A 67 38.23 36.93
REMARK 500 2 PRO A 79 39.86 -80.80
REMARK 500 2 THR B 4 32.51 -142.46
REMARK 500 2 LEU B 5 49.05 -85.55
REMARK 500 2 TRP B 6 52.57 17.84
REMARK 500 2 LEU B 24 103.90 -52.45
REMARK 500 2 ASP B 25 77.96 -101.16
REMARK 500 2 GLU B 34 166.69 -43.50
REMARK 500 2 GLN B 58 99.28 -48.42
REMARK 500 2 GLN B 61 63.77 71.49
REMARK 500 2 LEU B 63 85.71 -65.39
REMARK 500 2 PRO B 79 41.10 -79.57
REMARK 500 2 PRO B 81 21.52 -78.50
REMARK 500 3 GLN A 7 -99.04 -166.35
REMARK 500 3 LEU A 24 107.23 -46.86
REMARK 500 3 GLU A 34 153.34 -42.41
REMARK 500 3 GLN A 58 99.57 -60.67
REMARK 500 3 GLN A 61 60.33 82.01
REMARK 500 3 ALA A 71 99.72 -160.88
REMARK 500
REMARK 500 THIS ENTRY HAS 594 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 8 0.18 SIDE CHAIN
REMARK 500 1 ARG A 41 0.32 SIDE CHAIN
REMARK 500 1 ARG A 57 0.28 SIDE CHAIN
REMARK 500 1 ARG A 87 0.28 SIDE CHAIN
REMARK 500 1 ARG B 8 0.27 SIDE CHAIN
REMARK 500 1 ARG B 41 0.31 SIDE CHAIN
REMARK 500 1 ARG B 57 0.31 SIDE CHAIN
REMARK 500 1 ARG B 87 0.29 SIDE CHAIN
REMARK 500 2 ARG A 8 0.32 SIDE CHAIN
REMARK 500 2 ARG A 41 0.18 SIDE CHAIN
REMARK 500 2 ARG A 57 0.23 SIDE CHAIN
REMARK 500 2 ARG A 87 0.32 SIDE CHAIN
REMARK 500 2 ARG B 8 0.29 SIDE CHAIN
REMARK 500 2 ARG B 41 0.19 SIDE CHAIN
REMARK 500 2 ARG B 87 0.18 SIDE CHAIN
REMARK 500 3 ARG A 8 0.28 SIDE CHAIN
REMARK 500 3 ARG A 41 0.26 SIDE CHAIN
REMARK 500 3 ARG A 57 0.24 SIDE CHAIN
REMARK 500 3 ARG A 87 0.29 SIDE CHAIN
REMARK 500 3 ARG B 8 0.25 SIDE CHAIN
REMARK 500 3 ARG B 41 0.20 SIDE CHAIN
REMARK 500 3 ARG B 57 0.22 SIDE CHAIN
REMARK 500 3 ARG B 87 0.12 SIDE CHAIN
REMARK 500 4 ARG A 8 0.21 SIDE CHAIN
REMARK 500 4 ARG A 41 0.29 SIDE CHAIN
REMARK 500 4 ARG A 57 0.26 SIDE CHAIN
REMARK 500 4 ARG A 87 0.29 SIDE CHAIN
REMARK 500 4 ARG B 8 0.20 SIDE CHAIN
REMARK 500 4 ARG B 41 0.32 SIDE CHAIN
REMARK 500 4 ARG B 57 0.31 SIDE CHAIN
REMARK 500 4 ARG B 87 0.10 SIDE CHAIN
REMARK 500 5 ARG A 8 0.20 SIDE CHAIN
REMARK 500 5 ARG A 41 0.10 SIDE CHAIN
REMARK 500 5 ARG A 57 0.32 SIDE CHAIN
REMARK 500 5 ARG A 87 0.19 SIDE CHAIN
REMARK 500 5 ARG B 8 0.22 SIDE CHAIN
REMARK 500 5 ARG B 41 0.12 SIDE CHAIN
REMARK 500 5 ARG B 57 0.30 SIDE CHAIN
REMARK 500 5 ARG B 87 0.29 SIDE CHAIN
REMARK 500 6 ARG A 8 0.24 SIDE CHAIN
REMARK 500 6 ARG A 41 0.16 SIDE CHAIN
REMARK 500 6 ARG A 87 0.30 SIDE CHAIN
REMARK 500 6 ARG B 8 0.20 SIDE CHAIN
REMARK 500 6 ARG B 41 0.19 SIDE CHAIN
REMARK 500 6 ARG B 57 0.31 SIDE CHAIN
REMARK 500 6 ARG B 87 0.32 SIDE CHAIN
REMARK 500 7 ARG A 8 0.26 SIDE CHAIN
REMARK 500 7 ARG A 41 0.26 SIDE CHAIN
REMARK 500 7 ARG A 57 0.15 SIDE CHAIN
REMARK 500 7 ARG A 87 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 211 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMP B 100
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BVG RELATED DB: PDB
REMARK 900 REPRESENTATIVE STRUCTURE
DBREF 1BVE A 1 99 UNP P04585 POL_HV1H2 57 155
DBREF 1BVE B 1 99 UNP P04585 POL_HV1H2 57 155
SEQADV 1BVE ALA A 95 UNP P04585 CYS 151 ENGINEERED MUTATION
SEQADV 1BVE ALA B 95 UNP P04585 CYS 151 ENGINEERED MUTATION
SEQRES 1 A 99 PRO GLN VAL THR LEU TRP GLN ARG PRO LEU VAL THR ILE
SEQRES 2 A 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR
SEQRES 3 A 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO
SEQRES 4 A 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY
SEQRES 5 A 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU
SEQRES 6 A 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY
SEQRES 7 A 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR
SEQRES 8 A 99 GLN ILE GLY ALA THR LEU ASN PHE
SEQRES 1 B 99 PRO GLN VAL THR LEU TRP GLN ARG PRO LEU VAL THR ILE
SEQRES 2 B 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR
SEQRES 3 B 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO
SEQRES 4 B 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY
SEQRES 5 B 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU
SEQRES 6 B 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY
SEQRES 7 B 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR
SEQRES 8 B 99 GLN ILE GLY ALA THR LEU ASN PHE
HET DMP B 100 80
HETNAM DMP [4-R-(-4-ALPHA,5-ALPHA,6-BETA,7-BETA)]-HEXAHYDRO-5,6-
HETNAM 2 DMP BIS(HYDROXY)-[1,3-BIS([4-HYDROXYMETHYL-PHENYL]METHYL)-
HETNAM 3 DMP 4,7-BIS(PHEN YLMETHYL)]-2H-1,3-DIAZEPINONE
HETSYN DMP DMP323(INHIBITOR OF DUPONT MERCK)
FORMUL 3 DMP C35 H38 N2 O5
HELIX 1 1 ARG A 87 LEU A 90 1 4
HELIX 2 2 ARG B 87 LEU B 90 1 4
SHEET 1 A 3 LEU A 10 ILE A 13 0
SHEET 2 A 3 LYS A 20 LEU A 24 -1 N ALA A 22 O VAL A 11
SHEET 3 A 3 ASN A 83 ILE A 85 1 N ASN A 83 O LEU A 23
SHEET 1 B 2 THR A 31 LEU A 33 0
SHEET 2 B 2 VAL A 75 VAL A 77 1 N LEU A 76 O THR A 31
SHEET 1 C 2 TRP A 42 GLY A 48 0
SHEET 2 C 2 PHE A 53 TYR A 59 -1 N GLN A 58 O LYS A 43
SHEET 1 D 2 THR A 96 ASN A 98 0
SHEET 2 D 2 THR B 96 ASN B 98 -1 N ASN B 98 O THR A 96
SHEET 1 E 2 LEU B 10 ILE B 15 0
SHEET 2 E 2 GLN B 18 LEU B 23 -1 N ALA B 22 O VAL B 11
SHEET 1 F 3 VAL B 75 GLY B 78 0
SHEET 2 F 3 THR B 31 GLU B 34 1 N THR B 31 O LEU B 76
SHEET 3 F 3 ASN B 83 ILE B 85 -1 N ILE B 84 O VAL B 32
SHEET 1 G 2 LYS B 43 GLY B 48 0
SHEET 2 G 2 PHE B 53 GLN B 58 -1 N GLN B 58 O LYS B 43
SITE 1 AC1 17 ASP A 25 GLY A 27 ALA A 28 ASP A 29
SITE 2 AC1 17 GLY A 49 ILE A 50 PRO A 81 ILE A 84
SITE 3 AC1 17 ASP B 25 GLY B 27 ALA B 28 ASP B 29
SITE 4 AC1 17 ASP B 30 GLY B 49 ILE B 50 PRO B 81
SITE 5 AC1 17 ILE B 84
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - v 3 2 Bytes